This invention relates to novel peptides and, more particularly, to short synthetic peptides that block cell attachment to s-laminin.
S-laminin is a .about.190 kDa laminin-like glycoprotein that is concentrated in synaptic basal laminae. See Hunter et al, Nature 338, 229-234 (1989). S-laminin may play a role in the selective reinnervation of original synaptic sites and/or in the differentiation of axons into nerve terminals at these sites. This theory is supported by the homology of s-laminin to the .beta.1 subunit of laminin, which is known to be a major neurite outgrowth-promoting component of basal laminae.
It has been previously reported that neurons from embryonic chick ciliary ganglia adhere to a recombinant protein that consists of the C-terminal 40% of s-laminin fused to a 10 amino acid fragment of a phage capsid protein. See Hunter et al., supra. However, the essential motor neuron-attachment site of s-laminin has not been identified or described heretofore.